1fnl
From Proteopedia
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| , resolution 1.8Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF A HUMAN FCGRIII
Contents |
Overview
Fc receptors play a major role in immune defenses against pathogens and in inflammatory processes. The crystal structure of a human immunoglobulin receptor, FcgammaRIIIb, has been determined to 1.8 A resolution. The overall fold consists of two immunoglobulin-like domains with an acute interdomain hinge angle of approximately 50 degrees. Trp-113, wedged between the N-terminal D1 and the C-terminal D2 domains, appears to further restrict the hinge angle. The putative Fc binding region of the receptor carries a net positive charge complementary to the negative-charged receptor binding regions on Fc. A 1:1 binding stoichiometry between the receptor and Fc was measured by both the equilibrium and nonequilibrium size-exclusion chromatography. Two separate parallel dimers are observed in the crystal lattice, offering intriguing models for receptor aggregation.
Disease
Known diseases associated with this structure: Lupus erythematosus, systemic, susceptibility OMIM:[146740], Neutropenia, alloimmune neonatal OMIM:[146740], Viral infections, recurrent OMIM:[146740]
About this Structure
1FNL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the extracellular domain of a human Fc gamma RIII., Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD, Immunity. 2000 Sep;13(3):387-95. PMID:11021536
Page seeded by OCA on Thu Mar 20 11:11:30 2008
